Literature DB >> 21602342

Characterization of peptide chain length and constituency requirements for YejABEF-mediated uptake of microcin C analogues.

Gaston H M Vondenhoff1, Bart Blanchaert, Sophie Geboers, Teymur Kazakov, Kirill A Datsenko, Barry L Wanner, Jef Rozenski, Konstantin Severinov, Arthur Van Aerschot.   

Abstract

Microcin C (McC), a natural antibacterial compound consisting of a heptapeptide attached to a modified adenosine, is actively taken up by the YejABEF transporter, after which it is processed by cellular aminopeptidases, releasing the nonhydrolyzable aminoacyl adenylate, an inhibitor of aspartyl-tRNA synthetase. McC analogues with variable length of the peptide moiety were synthesized and evaluated in order to characterize the substrate preferences of the YejABEF transporter. It was shown that a minimal peptide chain length of 6 amino acids and the presence of an N-terminal formyl-methionyl-arginyl sequence are required for transport.

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Year:  2011        PMID： 21602342      PMCID： PMC3133342          DOI： 10.1128/JB.00172-11

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  18 in total

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  10 in total

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7.  The Novel Property of Heptapeptide of Microcin C7 in Affecting the Cell Growth of Escherichia coli.

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8.  Synthesis and Biological Evaluation of Lipophilic Nucleoside Analogues as Inhibitors of Aminoacyl-tRNA Synthetases.

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9.  N-alkylated aminoacyl sulfamoyladenosines as potential inhibitors of aminoacylation reactions and microcin C analogues containing D-amino acids.

Authors:  Gaston H Vondenhoff; Ksenia Pugach; Bharat Gadakh; Laurence Carlier; Jef Rozenski; Mathy Froeyen; Konstantin Severinov; Arthur Van Aerschot
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  10 in total

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